SPT6_SCHPO - dbPTM
SPT6_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT6_SCHPO
UniProt AC Q09915
Protein Name Transcription elongation factor spt6
Gene Name spt6
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1365
Subcellular Localization Nucleus .
Protein Description Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression (By similarity)..
Protein Sequence MSENEVVGSPTTNGDKNEDGYPAENGEGTNVDDNNNEEEKDGIPLDNDNDENDSSEESATDEEAERQVREGFIVEDEEDEVPQEIRRKKKRKKHAESTADQDMLDEEDLELVMENTGQGSRFSKLRRLKRGRDQEETLENIFSEEEEEEENEVDDEAPNRTQGHRAGVIDEFADFIEQDEFEDEERQEEKYETGPPIESVRPEALGISDDDYIQIYEVFGDGTDYAFALEDEDAEDELEESVSLKTIFEPSELKDKMLTEEDEIIRITDEPERMQLYMKRNIDCSEDEFREQVAWIIDYLLKNRRDIDAELYEPFQTAVRYVVHFFIRDSLEVPFIWQHRRDYIVHNNRERNTITPLLSQNDLWNIFFLCTKFWSLHSKKQDILKLYSDLGINDDLVVPFCEAASSLDAIDDLNDYIHFTYSEQIRDRALLMGTGLRRPQGSKYSFFEKFRKSSLYNLVKEFGMSAKDFSFNVAQGARLRFVEDNTLSPEELSRTYVTNELSSPEQVLQKARRVLAEEIIHDPQFRKSFRDKLYNAGVVTVLATQKGVRKIGSEHPYYEFKYLKRKPLGSFELEPILFLKMLKAEEEGLIQLSIEFEDPDDVFKGLLELFVSDNFSENAMQWNAQRELVLKEVFKRFSALAPDAIRETLRSRYLDELGMRCRNQLFSRLDQAPYEPSTKNFDRGTIPSVLAVSNGKGESSDAIICVFVDDVGEPTDSLKLADLRDLANQAMFAEFVEKVKPDVIGVSGMSVSAHKIRQHVQDSLTSHEPVDLIMVNDEVARLYQNSTRAVDEFPTLPTISCYCVALARYVQNPLFEYAAMGRDLMSLSFDPWQHLLPPDVLWKYLETALVDISSLVGIDINEAVTNKYEANILPYIAGLGPRKADYVLKKIAATGGRIDNRSDLISKQIMSRKVFINCSSFFIIPNDEYPNMDILDSTRIHNEDYELARKMASDALELDEEDIEELETNRGVVYHLLEENETGKLDELVLEEYADQLEREFHQKKRNTLEKIRLELKDPYGEQRNVFHKLTPSEIFLMLTGENPEELQADAIVPVNVRRVTNRFVAVKLDCGIDGNIKADEVSDDFIPPPQLLQVGQTVEGVIISLDEANFMVDLSLRNSVLQSANSKRQTSSHRTSYWDTEAEKRDTERMQAETQAEQRVARVIKHPLFKDLNASQAEAYLSKMQVGDLVIRPSSKGSDHIVVTWKVAEGSYQHIDVLELEKENEFTIGQKLLVKGRFEKMTYQYSDLDELIVLHIKAIAKKIDEMCIHDKFRKGTQAETEKWLESYSEANPKRSCYAFCFDHQHPGYFILCFKASVNSPVTAWPVKVIPNAFFLQGNVYGDMTALCNGFKLLYAARTKNFRRM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSENEVVGS
------CCCCCCCCC
61.5124763107
9PhosphorylationSENEVVGSPTTNGDK
CCCCCCCCCCCCCCC
13.8924763107
11PhosphorylationNEVVGSPTTNGDKNE
CCCCCCCCCCCCCCC
34.2921712547
137PhosphorylationRGRDQEETLENIFSE
CCCCHHHHHHHHCCH
38.3228889911
143PhosphorylationETLENIFSEEEEEEE
HHHHHHCCHHHHHHH
40.0628889911
454PhosphorylationFEKFRKSSLYNLVKE
HHHHHHHHHHHHHHH
37.6028889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SPT6_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT6_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPT6_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUT1_SCHPOcut1genetic
15507118
GCN5_SCHPOgcn5genetic
21844224
MST2_SCHPOmst2genetic
21844224
CENPA_SCHPOcnp1genetic
23028377
IWS1_SCHPOiws1physical
21844224
CLR3_SCHPOclr3genetic
23851719

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT6_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137; SER-143 ANDSER-454, AND MASS SPECTROMETRY.

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